1h4x
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(New page: 200px<br /> <applet load="1h4x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h4x, resolution 1.16Å" /> '''STRUCTURE OF THE BA...)
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Revision as of 17:34, 29 October 2007
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STRUCTURE OF THE BACILLUS CELL FATE DETERMINANT SPOIIAA IN THE PHOSPHORYLATED FORM
Overview
BACKGROUND: The asymmetric cell division during sporulation in Bacillus, subtilis gives rise to two compartments: the mother cell and the, forespore. Each follow different programs of gene expression coordinated, by a succession of alternate RNA polymerase sigma factors. The activity of, the first of these sigma factors, sigmaF, is restricted to the forespore, although sigmaF is present in the predivisional cell and partitions into, both compartments following the asymmetric septation. For sigmaF to become, active, it must escape from a complex with its cognate anti-sigma factor, SpoIIAB. This relief from SpoIIAB inhibition requires the, dephosphorylation of the anti-sigma factor antagonist, SpoIIAA. The, phosphorylation state of SpoIIAA is thus a key determinant of sigmaF, activity and ... [(full description)]
About this Structure
1H4X is a [Single protein] structure of sequence from [Bacillus sphaericus] with TRS as [ligand]. Full crystallographic information is available from [OCA].
Reference
Structure of the Bacillus cell fate determinant SpoIIAA in phosphorylated and unphosphorylated forms., Seavers PR, Lewis RJ, Brannigan JA, Verschueren KH, Murshudov GN, Wilkinson AJ, Structure. 2001 Jul 3;9(7):605-14. PMID:11470435
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